CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-017215
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Calcium-independent phospholipase A2-gamma 
Protein Synonyms/Alias
 Intracellular membrane-associated calcium-independent phospholipase A2 gamma; iPLA2-gamma; Patatin-like phospholipase domain-containing protein 8 
Gene Name
 Pnpla8 
Gene Synonyms/Alias
 Ipla22; Ipla2g 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
671TSTYTSLKTKLSNVIubiquitination[1]
Reference
 [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023] 
Functional Description
 Calcium-independent phospholipase A2, which catalyzes the hydrolysis of the sn-2 position of glycerophospholipids, PtdSer and to a lower extent PtdCho. Cleaves membrane phospholipids (By similarity). 
Sequence Annotation
 DOMAIN 439 634 Patatin.
 MOTIF 475 479 GXSXG (By similarity).
 CARBOHYD 4 4 N-linked (GlcNAc...) (Potential).
 CARBOHYD 157 157 N-linked (GlcNAc...) (Potential).  
Keyword
 Complete proteome; Cytoplasm; Endoplasmic reticulum; Glycoprotein; Golgi apparatus; Hydrolase; Lipid degradation; Lipid metabolism; Membrane; Reference proteome; Transmembrane; Transmembrane helix. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 776 AA 
Protein Sequence
MSINLTLDIY IYFLNNARSL CGKQRSKQLH FVCSKQYWRM NHVNVHREFH TSKKSCKWNR 60
SEAHCSKHWH SPSNHGLHFG IVRLSTSAPK GLTKVSIHMS RIKSTLNSVS KAIFGSQNEM 120
VTRLAQFKPS SRILRKVSDK GWLKQKNVKQ AVESLKNYSD KSAGKNSLAE QKSYFADKEE 180
DSGKHSLFHY TYGITTRFGE SFSVLANHIN SYFKSKGKMS QTKEDKQLQD KPDLEERKSS 240
SPGPDTVADR PDSESPLEVK DKLSSPTQMP EAHPVSAKQS IANFLSRPTE GVQALVGGYI 300
GGLVPKLKSD PKSPPEEQEV SAKTEQAVNK DKKAEEKKRV LLQQEKIIAR VSIDNRTRAL 360
VQALRRTADP KLCITRVEEL TFHLLEFPEG KGVAIKEKII PYLLRLRQVK DETLQAAVRE 420
ILALIGYVDP VKGRGIRILT IDGGGTRGVV ALQTLRKLVE LTQKPIHQLF DYICGVSTGA 480
ILAFMLGLFH MPLDECEELY RKLGSDVFTQ NVIVGTVKMS WSHAFYDSNT WEKILKDRIG 540
SALMIETARN PACPKVAAIS TIVNRGQTPK AFVFRNYGHF PGTNSHYLGG CQYKMWQAIR 600
ASSAAPGYFA EYALGSDLHQ DGGLLLNNPS ALALHECKCI WPDTPLECIV SLGTGRYESD 660
VRNTSTYTSL KTKLSNVISS ATDTEEVHIM LDGLLPSDTY FRFNPVICEN IPLDESRDEK 720
LDQLQLEGMK YIERNDQKMK KVAKILSQEK TTLQKINDWI KLKSDMYEGL PFFSKL 776 
Gene Ontology
 GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
 GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
 GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
 GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
 GO:0005778; C:peroxisomal membrane; ISS:UniProtKB.
 GO:0047499; F:calcium-independent phospholipase A2 activity; ISS:UniProtKB.
 GO:0004622; F:lysophospholipase activity; IEA:EC.
 GO:0019369; P:arachidonic acid metabolic process; IEA:Compara.
 GO:0050482; P:arachidonic acid secretion; IEA:Compara.
 GO:0008219; P:cell death; IEA:Compara.
 GO:0006631; P:fatty acid metabolic process; ISS:UniProtKB.
 GO:0043651; P:linoleic acid metabolic process; IEA:Compara.
 GO:0034638; P:phosphatidylcholine catabolic process; IEA:Compara.
 GO:0046338; P:phosphatidylethanolamine catabolic process; IEA:Compara.
 GO:0001516; P:prostaglandin biosynthetic process; IEA:Compara. 
Interpro
 IPR016035; Acyl_Trfase/lysoPLipase.
 IPR002641; Patatin/PLipase_A2-rel. 
Pfam
 PF01734; Patatin 
SMART
  
PROSITE
  
PRINTS